7BK8

X-ray crystal structure of Pseudomonas aeruginosa MagC

7BK8 の概要

• エントリーDOI: 10.2210/pdb7bk8/pdb
• 分子名称: MagC, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: alpha-2-macroglobulin, peptidoglycan, nlpc/p60, endopeptidase, hydrolase, magc
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24123.24

構造登録者

Zouhir, S.,Contreras-Martel, C.,Maragno Trindade, D.,Attree, I.,Dessen, A.,Macheboeuf, P. (登録日: 2021-01-15, 公開日: 2021-07-21, 最終更新日: 2024-06-19)

主引用文献

Zouhir, S.,Contreras-Martel, C.,Maragno Trindade, D.,Attree, I.,Dessen, A.,Macheboeuf, P.
MagC is a NplC/P60-like member of the alpha-2-macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan.
Febs Lett., 595:2034-2046, 2021

PubMed Abstract: Bacterial α-2 macroglobulins (A2Ms) structurally resemble the large spectrum protease inhibitors of the eukaryotic immune system. In Pseudomonas aeruginosa, MagD acts as an A2M and is expressed within a six-gene operon encoding the MagA-F proteins. In this work, we employ isothermal calorimetry (ITC), analytical ultracentrifugation (AUC), and X-ray crystallography to investigate the function of MagC and show that MagC associates with the macroglobulin complex and with the peptidoglycan (PG). However, the catalytic residues of MagC display an inactive conformation that could suggest that it binds to PG but does not degrade it. We hypothesize that MagC could serve as an anchor between the MagD macroglobulin and the PG and could provide stabilization and/or regulation for the entire complex.

PubMed: 34115884
DOI: 10.1002/1873-3468.14148

実験手法

X-RAY DIFFRACTION (1.74 Å)